Selective antibacterial activity of the cationic peptide PaDBS1R6 against Gram-negative bacteria

Fensterseifer, Isabel C. M.; Felício, Mário R.; Alves, E.S.F.; Cardoso, Marlon Henrique; Torres, Marcelo Der Torossian; Matos, Carolina O.; Silva, Osmar N.; Lu, Timothy K.; Freire, Maurício V.; Neves, Natan C.; Gonçalves, Sónia; Lião, Luciano M.; Santos, Nuno C.; Porto, William F.; Fuente-Núñez, César de la; Franco, Octávio Luiz

doi:10.1016/j.bbamem.2019.03.016

Cited by 45 publications

(37 citation statements)

References 87 publications

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“…A single dose (64 µM) of PaDBS1R6 was capable of reducing the initial bacterial load (∼10 8 CFU.mL −1 ) by up to three orders of magnitude after 2 days of treatment (Table 2). However, after four days of infection, the bacterial load increased for both peptide-treated and control animals, which might be related to degradation events in vivo (Fensterseifer et al, 2019).…”

Section: Automated Amino Acid Patterns Inserted Into Sequencesmentioning

confidence: 93%

“…PaDBS1R6F10 decreased the bacterial load gradually, reaching a reduction of ∼10 3 CFU.mL −1 after 4 days of treatment. Interestingly, this derivate exhibit improved in vivo activity when compared to the parental peptide PaDBS1R6, which did not maintain its anti-infective efficacy in vivo on the fourth day (Fensterseifer et al, 2019). According to the authors, this might suggest that the in vivo activity of these peptides (PaDBS1R6 and PaDBS1R6F10) is time-dependent and possibly involves peptide degradation events.…”

Section: Automated Amino Acid Patterns Inserted Into Sequencesmentioning

confidence: 99%

“…Based on the antimicrobial potential exhibited by the peptide PaDBS1R6 (Fensterseifer et al, 2019), and aiming at reducing this peptide's size, Cândido et al (2019) performed sliding window analysis, thus generating ten fragments derived from PaDBS1R6. As a result, the sliding window fragment PaDBS1R6F10 was the most active peptide at inhibiting bacterial growth, displaying activity toward E. coli (16-32 µM) and E. faecalis (4-8 µM) strains ( Table 2).…”

Section: Automated Amino Acid Patterns Inserted Into Sequencesmentioning

confidence: 99%

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Computer-Aided Design of Antimicrobial Peptides: Are We Generating Effective Drug Candidates?

et al. 2020

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Computer-Aided Design of Antimicrobial Peptides http://crdd.osdd.net/raghava/antibp2/ ClassAMP Uses RF and SVM to predict the propensity of a protein sequence to have antibacterial, antifungal, or antiviral activity http://www.bicnirrh.res.in/classamp/ AMPA Web tool for assessing the antimicrobial domains of proteins, with a focus on the design on new antimicrobial drugs http://tcoffee.crg.cat/apps/ampa/do DBAASP Provides users with information on detailed structure (chemical, 3D) and activity for those peptides, for which antimicrobial activity against particular target species have been evaluated experimentally https://dbaasp.org/home Joker An algorithm to design antimicrobial peptides using their language https://github.com/williamfp7/Joker

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Section: Automated Amino Acid Patterns Inserted Into Sequencesmentioning

confidence: 93%

Section: Automated Amino Acid Patterns Inserted Into Sequencesmentioning

confidence: 99%

Section: Automated Amino Acid Patterns Inserted Into Sequencesmentioning

confidence: 99%

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Computer-Aided Design of Antimicrobial Peptides: Are We Generating Effective Drug Candidates?

et al. 2020

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“…for PaDBS1R1 (11) and EcDBS1R5 (12). EcDBS1R6 (18) is also capable of killing Gram-positive bacteria, in addition to Gram-negatives (Table 1). Together with the absence of toxicity at antimicrobial concentrations, this peptide had a selective index of 12.92 against Gram-negative bacteria, which allows it to be considered as a safe drug, according to the U.S. Food and Drug Administration (19), especially due to its absence of toxicity to kidney cells (Table 1).…”

Section: Discussionmentioning

confidence: 99%

EcDBS1R6: A new broad-spectrum cationic antibacterial peptide derived from a signal peptide sequence

Porto

Irazazabal²,

Humblot

et al. 2019

Preprint

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Bacterial infections represent a major worldwide health problem, with an special highlight on Gram-negative bacteria, which were assigned by the World Health Organization (WHO) as the most critical priority for development of novel antimicrobial compounds. Antimicrobial peptides (AMPs) have been considered as potential alternative agents for treating these infections. Here we demonstrated the broad-spectrum activity of EcDBS1R6, a peptide derived from a signal peptide sequence of Escherichia coli that we previously turned into an AMP by making changes predicted through the Joker algorithm.Signal peptides are known to naturally interact with membranes; however, the modifications introduced by Joker made this peptide capable of killing bacteria. Membrane damage of the bacterial cells was observed by measuring membrane integrity using fluorescent probes and through scanning electron microscopy imaging. Structural analysis revealed that the C-terminus was unable to fold into an α -helix, indicating that the EcDBS1R6 antibacterial activity core was located at the N-terminus, corresponding to the signal peptide portion of the parent peptide. Therefore, the strategy of transforming signal peptides into AMPs seems to be promising and could be used for producing novel antimicrobial agents.

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“…For example, P. aeruginosa PAO1 bacterial strain is reported to be susceptible due to the presence of 2-amino-2,6-dideoxy-D-galactopyranose on LPS and P. aeruginosa ATCC 27853 strain is resistant to the antimicrobial peptide (AMP) by the absence of LPS B-band [58]. Also, the presence of cardiolipin appears to be a determinant for AMP antibacterial activity against Gram-negative bacteria [59]. Likewise, DMS-DA6 peptides act by strong perturbation of the bacterial membrane against the Grampositive bacteria S. aureus ATCC 6538 but not against the Gram-negative bacteria E. coli ATCC 35218 because of specificity DMS-DA6 interaction with peptidoglycan, a major component of the membrane of Gram-positive bacteria [60].…”

Section: Small Intestine Submucosamentioning

confidence: 99%

Antimicrobial Properties of Extracellular Matrix Scaffolds for Tissue Engineering

Jiménez-Gastélum

Aguilar-Medina

Soto-Sáinz

et al. 2019

BioMed Research International

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The necessity to manufacture graft materials with superior biocompatibility capabilities and biodegradability characteristics for tissue regeneration has led to the production of extracellular matrix- (ECM-) based scaffolds. Among their advantages are better capacity to allow cell colonization, which enables its successful integration into the tissue surrounding the area to be repaired. In addition, it has been shown that some of these scaffolds have antimicrobial activity, preventing possible infections; therefore, it could be used as an alternative to control surgical infection and decrease the use of antimicrobial agents. The purpose of this review is to collect the existing information about antimicrobial activity of the ECM and their components.

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Selective antibacterial activity of the cationic peptide PaDBS1R6 against Gram-negative bacteria

Cited by 45 publications

References 87 publications

Computer-Aided Design of Antimicrobial Peptides: Are We Generating Effective Drug Candidates?

Computer-Aided Design of Antimicrobial Peptides: Are We Generating Effective Drug Candidates?

EcDBS1R6: A new broad-spectrum cationic antibacterial peptide derived from a signal peptide sequence

Antimicrobial Properties of Extracellular Matrix Scaffolds for Tissue Engineering

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